XB31_ARATH
ID XB31_ARATH Reviewed; 456 AA.
AC Q94B55; Q56W24; Q944L4; Q9ZV30;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Putative E3 ubiquitin-protein ligase XBAT31;
DE EC=2.3.2.27;
DE AltName: Full=Ankyrin repeat domain and RING finger-containing protein XBAT31;
DE AltName: Full=Protein XB3 homolog 1;
DE AltName: Full=RING-type E3 ubiquitin transferase XB31;
GN Name=XBAT31; OrderedLocusNames=At2g28840; ORFNames=F8N16.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Seed;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-456.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: No E3 ubiquitin-protein ligase activity observed when
CC associated with the E2 enzyme UBC8 in vitro.
CC {ECO:0000269|PubMed:15644464}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94B55-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79588.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL16133.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD95395.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ086863; AAZ14079.1; -; mRNA.
DR EMBL; AC005727; AAC79588.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08179.1; -; Genomic_DNA.
DR EMBL; AF370581; AAK49587.1; -; mRNA.
DR EMBL; AF428301; AAL16133.1; ALT_SEQ; mRNA.
DR EMBL; AY042842; AAK68782.1; -; mRNA.
DR EMBL; AY081458; AAM10020.1; -; mRNA.
DR EMBL; BT000727; AAN31869.1; -; mRNA.
DR EMBL; AK222223; BAD95395.1; ALT_INIT; mRNA.
DR PIR; E84689; E84689.
DR RefSeq; NP_180450.2; NM_128443.4. [Q94B55-1]
DR AlphaFoldDB; Q94B55; -.
DR SMR; Q94B55; -.
DR BioGRID; 2783; 2.
DR IntAct; Q94B55; 2.
DR STRING; 3702.AT2G28840.1; -.
DR PaxDb; Q94B55; -.
DR PRIDE; Q94B55; -.
DR EnsemblPlants; AT2G28840.1; AT2G28840.1; AT2G28840. [Q94B55-1]
DR GeneID; 817433; -.
DR Gramene; AT2G28840.1; AT2G28840.1; AT2G28840. [Q94B55-1]
DR KEGG; ath:AT2G28840; -.
DR Araport; AT2G28840; -.
DR TAIR; locus:2053205; AT2G28840.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_049095_1_0_1; -.
DR InParanoid; Q94B55; -.
DR OMA; CTIEVQS; -.
DR PhylomeDB; Q94B55; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94B55; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94B55; baseline and differential.
DR Genevisible; Q94B55; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Metal-binding; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..456
FT /note="Putative E3 ubiquitin-protein ligase XBAT31"
FT /id="PRO_0000395739"
FT REPEAT 45..74
FT /note="ANK 1"
FT REPEAT 78..107
FT /note="ANK 2"
FT REPEAT 112..141
FT /note="ANK 3"
FT REPEAT 157..186
FT /note="ANK 4"
FT REPEAT 194..224
FT /note="ANK 5"
FT ZN_FING 319..368
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 229
FT /note="R -> S (in Ref. 5; BAD95395)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="A -> V (in Ref. 5; BAD95395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49610 MW; 83C4ACE71A827E72 CRC64;
MGQSMSCGSR PEHGIFASVQ CGDIITIRRV MATEPSLLNQ TTPYDRHSVL HVAAANGQIE
ILSLLLERFT NPDLLNRHKQ TPLMLAAMYG RISCVKKLAE VGANILMFDS VNRRTCLHYA
AYYGHANCVQ AILSAAQSSP VAVHWGYARF VNIRDDKGAT PLHLAARQRR PECVNVLLDS
GSLVCASTSV YGSPGSTPLH LAARSGSIDC VRKLLAWGAD RLQRDASGRI PYVVAMKHKH
GACGALLNPS SAEPLVWPSP LKFISELNDE AKLLLEQALM EANREREKTI LKGTAYSLPS
PSFSDTDDNM SEVSDTELCC ICFEQVCTIE VKDCGHQMCA QCTLALCCHN KPNPTTSTVT
PPVCPFCRST IACLVVAQNN NNNNEKSKSL DDVVVVDREA GDVSSSKFRK HRRSINLGEE
SSSFMGLSTI GSFGRITGRG SGRIAAENEL MDKPIL
